Identification of the Amino Acid Residues Conferring Substrate Specificity uponSelenomonas ruminantiumLysine Decarboxylase | Zendy

Yumiko Takatsuka | Zendy; Noriko Tomita | Zendy; Yoshiyuki Kamio | Zendy

Open Access

Identification of the Amino Acid Residues Conferring Substrate Specificity uponSelenomonas ruminantiumLysine Decarboxylase

Author(s) -

Yumiko Takatsuka,

Noriko Tomita,

Yoshiyuki Kamio

Publication year - 1999

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.63.1843

Subject(s) - lysine , lysine decarboxylase , ornithine decarboxylase , biochemistry , enzyme , residue (chemistry) , ornithine , amino acid , substrate (aquarium) , amino acid residue , biology , chemistry , peptide sequence , arginine , gene , ecology , putrescine , cadaverine

Lysine decarboxylase (LDC, EC 4.1.1.18) from Selenomonas ruminantium has decarboxylating activities towards both L-lysine and L-ornithine with similar K(m) and Vmax. Here, we identified four amino acid residues that confer substrate specificity upon S. ruminantium LDC and that are located in its catalytic domain. We have succeeded in converting S. ruminantium LDC to an enzyme with a preference in decarboxylating activity for L-ornithine when the four-residue of LDC were replaced by the corresponding residues of mouse ornithine decarboxylase (EC 4.1.1.17).

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research